The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S-peptide analogues with enhanced helical stability-Reference-Cited by-同舟云学术

The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S-peptide analogues with enhanced helical stability

Published:1986-01 Issue:1 Volume:1 Page:23-33
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Genetics
language:en
Short-container-title:Proteins

Author:

Mitchinson Colin,Baldwin Robert L.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference39 articles.

1. Thermodynamics of protein cross-links

2. Influence of an extrinsic crosslink on the folding pathway of ribonuclease A. Conformational and thermodynamic analysis of crosslinked (7-lysine, 41-lysine)-ribonuclease A

3. Directed Mutagenesis of Dihydrofolate Reductase

4. Disulfide Bond Engineered into T4 Lysozyme: Stabilization of the Protein Toward Thermal Inactivation

5. The Preparation of Subtilisin-modified Ribonuclease and the Separation of the Peptide and Protein Components

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